Nucleic Acids Research, Vol 25, Issue 2 423-430, Copyright © 1997 by Oxford University Press
B Chen, BH Han, XH Sun and RW Lim
We have examined the role of an Id-like protein, Id3 (also known as
HLH462), in the regulation of muscle-specific gene expression. Id proteins
are believed to block expression of muscle-specific genes by preventing the
dimerization between ubiquitous bHLH proteins (E proteins) and myogenic
bHLH proteins such as MyoD. Consistent with its putative role as an
inhibitor of differentiation, Id3 mRNA was detected in proliferating
skeletal muscle cells, was further induced by basic fibroblast growth
factor (bFGF) and was down-regulated in differentiated muscle cultures.
Overexpression of Id3 efficiently inhibited the MyoD-mediated activation of
the muscle-specific creatine kinase (MCK) reporter gene. Deletion analysis
indicated that the C- terminal 15 amino acids of Id3 are critical for the
full inhibitory activity while deleting up to 42 residues from the
C-terminus of the related protein, Id2, did not affect its ability to
inhibit the MCK reporter gene. Chimeric protein containing the N-terminal
region of Id3 and the C-terminus of Id2 was also non-functional in
transfected cells. In contrast, wild-type Id3, the C-terminal mutants, and
the Id3/Id2 chimera could all interact with the E-protein E47in vitro.
Additional studies indicated that truncation of the Id3 C-terminus might
have adversely affected the expression level of the mutant proteins but the
Id3/Id2 chimera was stably expressed. Taken together, our results revealed
a more complex requirement for the expression and proper function of the Id
family proteins than was hitherto expected.
ARTICLES
Inhibition of muscle-specific gene expression by Id3: requirement of the C-terminal region of the protein for stable expression and function
Department of Pharmacology, School of Medicine, University of Missouri, Columbia, MO 65212, USA.
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